Purification and properties of superoxide dismutase from Thermus thermophilus HB8.
Purification and properties of superoxide dismutase from Thermus thermophilus HB8.
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嗜热栖热菌 HB8 超氧化物歧化酶的纯化和性质。
DOI：
10.1093/oxfordjournals.jbchem.a132007
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发表时间：
1978
影响因子：
2.7
通讯作者：
K. Nakazawa
中科院分区：
文献类型：
--
作者：
S. Sato;K. Nakazawa
含锰超氧化物歧化酶是从极端嗜热菌Thermus thermophilus HB 8中分离得到的。从500 g湿细胞中获得约150 mg酶。该酶在硫酸铵溶液中易结晶为八面体。经沉降平衡法和凝胶过滤法测得该酶的分子量分别为8.2 × 10 ~（4）和8.4 × 10 ~（4）。这种酶每摩尔含有2个锰原子，由4个分子量相同的亚基组成，约为2.1 × 10（4）。该酶的氨基酸组成与水生栖热菌超氧化物歧化酶的氨基酸组成相似。脯氨酸被检测为N-末端氨基酸。通过电聚焦法测定等电点为pH 6.0。该酶在283 nm和480 nm处有最大吸收。CD光谱表明该酶具有高α-螺旋含量。
Manganese-containing superoxide dismutase was isolated from an extreme thermophile, Thermus thermophilus HB8. About 150 mg of the enzyme was obtained from 500 g of wet cells. The enzyme was easily crystallized in octahedra from ammonium sulfate solution. The molecular weight of the enzyme was determined to be 8.2 X 10(4) and 8.4 X 10(4) by sedimentation equilibrium and gel-filtration, respectively. The enzyme contains 2 atoms of manganese per mole and consists of four subunits of identical molecular weight, about 2.1 X 10(4). The amino acid composition of the enzyme is similar to that of the superoxide dismutase of Thermus aquaticus. Proline was detected as the N-terminal amino acid. The isoelectric point was determined to be pH 6.0 by the electrofocusing method. The enzyme has maxima at 283 nm and 480 nm in the absorption spectrum. The CD spectrum suggests that the enzyme has a high alpha-helical content.